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1lmp

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Revision as of 07:44, 31 January 2018

THE CRYSTAL STRUCTURES OF THREE COMPLEXES BETWEEN CHITOOLIGOSACCHARIDES AND LYSOZYME FROM THE RAINBOW TROUT

Structural highlights

1lmp is a 1 chain structure with sequence from Oncorhynchus mykiss. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Lysozyme, with EC number 3.2.1.17
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LYSC2_ONCMY] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has antibacterial activity against the Gram positive bacterium P.citreus. Has no antibacterial activity against the Gram negative bacteria E.coli and Y.ruckeri. Does not have hemolytic activity against trout erythrocytes.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Like all c-type lysozymes, those from rainbow trout act as 1,4-beta-acetyl-muramidases to destroy bacteria by cleaving the polysaccharide chains of alternating N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) units in the cell walls. Lysozymes also hydrolyse chitin, the analogous N-acetylglucosamine polymer. The rainbow trout enzymes have been shown to be particularly effective in bacterial defence. We have determined the crystal structures of three complexes between rainbow trout lysozyme (RBTL) and the chito-oligosaccharides (NAG)(2), (NAG)(3) and (NAG)(4) to resolutions of 1.8, 2.0 and 1.6 A, respectively. Crystals of these complexes were obtained by co-crystallization, and intensity data were collected on a FAST area detector system. Refinement and model building gave final R values of 16.6, 15.9 and 16.5% for the di-, tri- and tetrasaccharide complexes, respectively. The results show that the chito-oligosaccharides bind to sites A, B and C as previously observed for complexes between the hen egg-white lysozyme (HEWL) and a variety of saccharides. The NAG ring in site D is not bound so deeply and is only slightly distorted towards a half-chair conformation as observed for the equivalent NAM residue in HEWL. From our results, there is reason to question the position and the degree of strain of the D saccharide and the mode of binding and importance of two saccharides in sites E and F for correct orientation of sugar D and effective hydrolysis of a productive substrate-lysozyme complex. Simple model building study from our structures implies a 'left-sided' binding mode of (NAG)(6) in the lower part of the active site of RBTL.

Crystal structures of three complexes between chito-oligosaccharides and lysozyme from the rainbow trout. How distorted is the NAG sugar in site D?,Karlsen S, Hough E Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):962-78. PMID:15299765^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fernandes JM, Kemp GD, Smith VJ. Two novel muramidases from skin mucosa of rainbow trout (Oncorhynchus mykiss). Comp Biochem Physiol B Biochem Mol Biol. 2004 May;138(1):53-64. PMID:15142536 doi:http://dx.doi.org/10.1016/j.cbpc.2004.02.004
↑ Karlsen S, Hough E. Crystal structures of three complexes between chito-oligosaccharides and lysozyme from the rainbow trout. How distorted is the NAG sugar in site D? Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):962-78. PMID:15299765 doi:10.1107/S0907444995005105

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lmp"

Categories: Lysozyme | Oncorhynchus mykiss | Hough, E | Karlsen, S

@@ Line 1: / Line 1: @@
 ==THE CRYSTAL STRUCTURES OF THREE COMPLEXES BETWEEN CHITOOLIGOSACCHARIDES AND LYSOZYME FROM THE RAINBOW TROUT==
 <StructureSection load='1lmp' size='340' side='right' caption='[[1lmp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmp OCA], [http://pdbe.org/1lmp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lmp RCSB], [http://www.ebi.ac.uk/pdbsum/1lmp PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmp OCA], [http://pdbe.org/1lmp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lmp RCSB], [http://www.ebi.ac.uk/pdbsum/1lmp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lmp ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lm/1lmp_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lm/1lmp_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1lmp" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 == References ==
 <references/>

1lmp

From Proteopedia

Revision as of 07:44, 31 January 2018

THE CRYSTAL STRUCTURES OF THREE COMPLEXES BETWEEN CHITOOLIGOSACCHARIDES AND LYSOZYME FROM THE RAINBOW TROUT

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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